ID A0A238K4D1_9RHOB Unreviewed; 988 AA.
AC A0A238K4D1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN Name=sucA {ECO:0000313|EMBL:SMX37254.1};
GN ORFNames=PEV8663_00994 {ECO:0000313|EMBL:SMX37254.1};
OS Pelagimonas varians.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pelagimonas.
OX NCBI_TaxID=696760 {ECO:0000313|EMBL:SMX37254.1, ECO:0000313|Proteomes:UP000220836};
RN [1] {ECO:0000313|EMBL:SMX37254.1, ECO:0000313|Proteomes:UP000220836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8663 {ECO:0000313|EMBL:SMX37254.1,
RC ECO:0000313|Proteomes:UP000220836};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC dehydrogenase); the complex contains multiple copies of the three
CC enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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DR EMBL; FXYH01000003; SMX37254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238K4D1; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000220836; Unassembled WGS sequence.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SMX37254.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000220836};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 632..825
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 110391 MW; A3512BE06871E6C0 CRC64;
MTDQSPNDLF QASSFMQGHN AEYLEQMYAR YASDPNAVDQ AWQEFFRQLG DADLDVKAEA
QGPSWARNDW PQQPSDELTS ALTGEWAPAP AETKGAGKKI KAQAEAKGVT LTDDQVQRAV
LDSIRALMLI RAYRIRGHLA ADLDPLGLHG REPHPELDPK SYGFTDADMD RPIFIDNVLG
LQIASMRQIV EIVKRTYCGT FALQYMHISD PEQAAWLKER IEGFGKEIAF TREGRKAILN
KMVEAEGFEK FLHVKYMGTK RFGLDGGESL IPAMEQIIKR GGNLGVRDIV IGMPHRGRLS
VLANVMAKPY KAIFNEFQGG SSKPEDVDGS GDVKYHLGAS SDREFDGNSV HLSLTANPSH
LEAVNPVVLG KVRAKQDQLN DDDRMSVMPI LLHGDAAFAG QGVVAECFAL SGLRGHKTGG
TMHIVVNNQI GFTTAPHFSR SSPYPTDNAL VVEAPIFHVN GDDPEAVVHA AKVATEYRQK
FHRDVVIDIF CYRRFGHNEG DEPMFTNPIM YKQIKSHKTT LSLYTERLVK DGLIPEGEIE
DMKAAFQAHL NEEFEAGKAY KPNKADWLDG RWSHLDRQQQ GKYQRGKTAI ASEAAKDIGT
ALTRVPEGFP LHKTVGRLVD TRAKMFETGK GFDWATGEAL AFGSLQLEGY PIRLAGQDST
RGTFSQRHSG FVNQETEERY YPLNNIREGQ ARYEVIDSAL SEYAVLGFEY GYSLAEPNAL
TLWEAQFGDF ANGAQIMFDQ FVSSGESKWL RMSGLVCLLP HGFEGQGPEH SSARLERFLQ
MCGQDNWIVA NCSTPANYFH ILRRQLHRSF RKPLIMVTPK SLLRHKLCTS AIEDFTEGSS
FHRVLWDDAE KGQSDTVLKA DDKIKRVVMC SGKVYYDLLE ERDARGIDDI YLLRVEQFYP
FPALALVKEL ERFPGAEMVW CQEEPKNQGA WTFIEPNIEW VLGRIKATHQ RPVYVGRATS
ASPATGLASI HKAQQAALVN EALTIEGN
//
